MolNFT v1 · #99373 · protein

Crystal structure of elongation factor G (efg)

4M1K: “Crystal structure of elongation factor G (efg)”. X-ray diffraction, 2 ligands (GDP, MG), 8 pockets (best druggability 0.77). MolNFT v1 #99373 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4M1K
Type: protein
Length: 656 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor G
UniProt: P13551
Ligands: GDP, MG
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor G	protein	656	27% helix, 33% strand	P13551

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	868	0.77	0.80	68	empty
2	54	0.68	0.97	23	empty
3	86	0.68	0.93	20	empty
4	170	0.52	0.78	25	empty
5	187	0.46	0.75	25	empty

Compared structures

4M1K · Crystal structure of elongation factor G (EFG) · the same entry in another collection · chain A against A, TM-score 1.00
P13551 · AlphaFold monomer V2.0 prediction for elongation factor G (P13551) · a predicted model of the same protein · chain A against A, TM-score 0.76

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P13551
Elsewhere: RCSB PDB 4M1K · PDBe 4M1K · UniProt P13551

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